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Protein

Pyruvate kinase

Gene

pyk

Organism
Lactobacillus delbrueckii subsp. bulgaricus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Strongly activated by glucose-6-phosphate, ribose-5-phosphate and fructose-6-phosphate. Weak activator AMP and weak inhibitor fructose-1,6-bisphosphate can act as strong inhibitors in the presence of strong activators.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei32 – 321SubstrateBy similarity
Metal bindingi34 – 341PotassiumBy similarity
Metal bindingi36 – 361PotassiumBy similarity
Metal bindingi66 – 661PotassiumBy similarity
Metal bindingi67 – 671Potassium; via carbonyl oxygenBy similarity
Sitei221 – 2211Transition state stabilizerBy similarity
Metal bindingi223 – 2231MagnesiumBy similarity
Binding sitei246 – 2461Substrate; via amide nitrogenBy similarity
Metal bindingi247 – 2471MagnesiumBy similarity
Binding sitei247 – 2471Substrate; via amide nitrogenBy similarity
Binding sitei279 – 2791SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Pyruvate

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate kinase (EC:2.7.1.40)
Short name:
PK
Gene namesi
Name:pyk
OrganismiLactobacillus delbrueckii subsp. bulgaricus
Taxonomic identifieri1585 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 589589Pyruvate kinasePRO_0000112076Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi390333.Ldb0839.

Structurei

3D structure databases

ProteinModelPortaliP34038.
SMRiP34038. Positions 1-589.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pyruvate kinase family.Curated
In the C-terminal section; belongs to the PEP-utilizing enzyme family.Curated

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
3.50.30.10. 1 hit.
InterProiIPR008279. PEP-util_enz_mobile_dom.
IPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015794. Pyrv_Knase_a/b.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
IPR015806. Pyrv_Knase_insert_dom.
[Graphical view]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00391. PEP-utilizers. 1 hit.
PF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.

Sequencei

Sequence statusi: Complete.

P34038-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKTKIVSTL GPASDDIETI TKLAEAGANV FRFNFSHGNH EEHLARMNMV
60 70 80 90 100
REVEKKTGKL LGIALDTKGA EIRTTDQEGG KFTINTGDEI RVSMDATKAG
110 120 130 140 150
NKDMIHVTYP GLFDDTHVGG TVLIDDGAVG LTIKAKDEEK RELVCEAQNT
160 170 180 190 200
GVIGSKKGVN APGVEIRLPG ITEKDTDDIR FGLKHGINFI FASFVRKAQD
210 220 230 240 250
VLDIRALCEE ANASYVKIFP KIESQEGIDN IDEILQVSDG LMVARGDMGV
260 270 280 290 300
EIPFINVPFV QKTLIKKCNA LGKPVITATQ MLDSMQENPR PTRAEVTDVA
310 320 330 340 350
NAVLDGTDAT MLSGESANGL YPVQSVQAMH DIDVRTEKEL DTRNTLALQR
360 370 380 390 400
FEEYKGSNVT EAIGESVVRT AQELGVKTII AATSSGYTAR MISKYRPDAT
410 420 430 440 450
IVALTFDEKI QHSLGIVWGV EPVLAKKPSN TDEMFEEAAR VAKEHGFVKD
460 470 480 490 500
GDLVIIVAGV PFGQSGTTNL MKLQIIGNQL AQGLGVGTGS VIGKAVVANS
510 520 530 540 550
AEEANAKVHE GDILVAKTTD KDYMPAIKKA SGMIVEASGL TSHAAVVGVS
560 570 580
LGIPVVVGVA DATSKIADGS TLTVDARRGA IYQGEVSNL
Length:589
Mass (Da):62,920
Last modified:February 1, 1996 - v3
Checksum:i2BA3D3CF7AE290F1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71403 Genomic DNA. Translation: CAA50527.1.
PIRiB48663.
S35929.
RefSeqiWP_003619815.1. NZ_CCEU01000003.1.

Genome annotation databases

GeneIDi4084389.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71403 Genomic DNA. Translation: CAA50527.1.
PIRiB48663.
S35929.
RefSeqiWP_003619815.1. NZ_CCEU01000003.1.

3D structure databases

ProteinModelPortaliP34038.
SMRiP34038. Positions 1-589.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi390333.Ldb0839.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi4084389.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
3.50.30.10. 1 hit.
InterProiIPR008279. PEP-util_enz_mobile_dom.
IPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015794. Pyrv_Knase_a/b.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
IPR015806. Pyrv_Knase_insert_dom.
[Graphical view]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00391. PEP-utilizers. 1 hit.
PF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The genes for phosphofructokinase and pyruvate kinase of Lactobacillus delbrueckii subsp. bulgaricus constitute an operon."
    Branny P., de la Torre F., Garel J.R.
    J. Bacteriol. 178:4727-4730(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cloning, sequencing, and expression in Escherichia coli of the gene coding for phosphofructokinase in Lactobacillus bulgaricus."
    Branny P., de la Torre F., Garel J.R.
    J. Bacteriol. 175:5344-5349(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60.
  3. "Pyruvate kinase from Lactobacillus bulgaricus: possible regulation by competition between strong and weak effectors."
    le Bras G., Garel J.R.
    Biochimie 75:797-802(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-40, CHARACTERIZATION.

Entry informationi

Entry nameiKPYK_LACDE
AccessioniPrimary (citable) accession number: P34038
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1996
Last modified: June 24, 2015
This is version 99 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.